Fig. 6

a Predicted β-defensin domain model for Odonus niger β-defensin (On-Def) by I-TASSER. The three β-strands are denoted yellow with the three disulfide bonds (blue) stabilizing the β-defensin fold. The C-terminal β-strand (β3) is trapped between the other two β strands (β1 and β2) by the β-hairpin G⁴⁸–Y⁵⁶ (green) forming the typical anti-parallel β-defensin structure. b The buried position of cysteine residues with their disulfide bonds were computed using the accessibility color tool of Swiss PDB Viewer 4.1, which displays accessibility of residues ranging from deep blue (most buried) to red (most exposed)